位置:首页 > 蛋白库 > MSRP_ANAD2
MSRP_ANAD2
ID   MSRP_ANAD2              Reviewed;         313 AA.
AC   B8J9Q0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Protein-methionine-sulfoxide reductase catalytic subunit MsrP {ECO:0000255|HAMAP-Rule:MF_01206};
DE            EC=1.8.5.- {ECO:0000255|HAMAP-Rule:MF_01206};
DE   Flags: Precursor;
GN   Name=msrP {ECO:0000255|HAMAP-Rule:MF_01206}; OrderedLocusNames=A2cp1_4120;
OS   Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=455488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-1 / ATCC BAA-258;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Beliaev A.S., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the MsrPQ system that repairs oxidized periplasmic
CC       proteins containing methionine sulfoxide residues (Met-O), using
CC       respiratory chain electrons. Thus protects these proteins from
CC       oxidative-stress damage caused by reactive species of oxygen and
CC       chlorine generated by the host defense mechanisms. MsrPQ is essential
CC       for the maintenance of envelope integrity under bleach stress, rescuing
CC       a wide series of structurally unrelated periplasmic proteins from
CC       methionine oxidation. The catalytic subunit MsrP is non-stereospecific,
CC       being able to reduce both (R-) and (S-) diastereoisomers of methionine
CC       sulfoxide. {ECO:0000255|HAMAP-Rule:MF_01206}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H2O + L-methionyl-[protein] = a quinol + L-
CC         methionyl-(S)-S-oxide-[protein]; Xref=Rhea:RHEA:51292, Rhea:RHEA-
CC         COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16044, ChEBI:CHEBI:24646, ChEBI:CHEBI:44120,
CC         ChEBI:CHEBI:132124; Evidence={ECO:0000255|HAMAP-Rule:MF_01206};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H2O + L-methionyl-[protein] = a quinol + L-
CC         methionyl-(R)-S-oxide-[protein]; Xref=Rhea:RHEA:51296, Rhea:RHEA-
CC         COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16044, ChEBI:CHEBI:24646, ChEBI:CHEBI:45764,
CC         ChEBI:CHEBI:132124; Evidence={ECO:0000255|HAMAP-Rule:MF_01206};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01206};
CC       Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_01206};
CC   -!- SUBUNIT: Heterodimer of a catalytic subunit (MsrP) and a heme-binding
CC       subunit (MsrQ). {ECO:0000255|HAMAP-Rule:MF_01206}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01206}.
CC       Note=Is attached to the inner membrane when interacting with the MsrQ
CC       subunit. {ECO:0000255|HAMAP-Rule:MF_01206}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC       {ECO:0000255|HAMAP-Rule:MF_01206}.
CC   -!- SIMILARITY: Belongs to the MsrP family. {ECO:0000255|HAMAP-
CC       Rule:MF_01206}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001359; ACL67438.1; -; Genomic_DNA.
DR   RefSeq; WP_015935157.1; NC_011891.1.
DR   AlphaFoldDB; B8J9Q0; -.
DR   SMR; B8J9Q0; -.
DR   EnsemblBacteria; ACL67438; ACL67438; A2cp1_4120.
DR   KEGG; acp:A2cp1_4120; -.
DR   HOGENOM; CLU_045520_0_0_7; -.
DR   OMA; WPYTEGL; -.
DR   Proteomes; UP000007089; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016672; F:oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.420.10; -; 1.
DR   HAMAP; MF_01206; MsrP; 1.
DR   InterPro; IPR022867; MsrP.
DR   InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR   InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF00174; Oxidored_molyb; 1.
DR   SUPFAM; SSF56524; SSF56524; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Molybdenum; Oxidoreductase; Periplasm; Signal.
FT   SIGNAL          1..44
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT   CHAIN           45..313
FT                   /note="Protein-methionine-sulfoxide reductase catalytic
FT                   subunit MsrP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT                   /id="PRO_1000164653"
FT   BINDING         76
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT   BINDING         79..80
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT   BINDING         134
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT   BINDING         169
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT   BINDING         217
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT   BINDING         222
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT   BINDING         233..235
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
SQ   SEQUENCE   313 AA;  35282 MW;  EC13EC3EB6CF0EAC CRC64;
     MARWRPDMAE REATPEALYL RRRDFLALGA AGAVGLLLPR GARAGDPTGA ALQVARKVDQ
     AGGETPTPWD SVTGYNNFYE LGTSKEDPSR NAGSLRARPW TVTIAGEVKR PQTLDVDALV
     RMFPPEERVY RMRCVEAWSM VIPWVGFPLA DLVRRLEPTS RAKYVAFQTL LDRDQLPGQR
     RPVLPWPYVE ALRIDEANHP LALLAVGLYG RVLPGQNGAP LRLVVPWKYG FKGAKSIVRI
     TFLADRPHTT WNDAAPDEYG FYANVNPEVD HPRWSQARER RIGEFFRRKT LPFNGYAAEV
     APLYAGLDLR KNY
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024